Structure of PDB 2rdw Chain A

Receptor sequence
>2rdwA (length=359) Species: 9606 (Homo sapiens) [Search protein sequence]
RLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRM
LRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGT
GMMLSSWATSSIEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYK
AIFVTVDTPYLGNRLDDVRNRFKLPPQLRMKNFETSTLSFSPEENFGDDS
GLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVKHGLN
GILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKA
LALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVK
VIDKTLVRK
3D structure
PDB2rdw Active Site and Loop 4 Movements within Human Glycolate Oxidase: Implications for Substrate Specificity and Drug Design.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S108 Y132 T158 D160 K236 H260
Catalytic site (residue number reindexed from 1) S105 Y129 T155 D157 K233 H257
Enzyme Commision number 1.1.3.15: (S)-2-hydroxy-acid oxidase.
1.2.3.5: glyoxylate oxidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SO4 A Y26 W110 R167 H260 R263 Y23 W107 R164 H257 R260
BS02 FMN A Y26 Y27 A79 T80 A81 Q130 Y132 T158 K236 H260 G261 R263 D291 G292 R295 G314 R315 Y23 Y24 A76 T77 A78 Q127 Y129 T155 K233 H257 G258 R260 D288 G289 R292 G311 R312
Gene Ontology
Molecular Function
GO:0003973 (S)-2-hydroxy-acid oxidase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0047969 glyoxylate oxidase activity
Biological Process
GO:0001561 fatty acid alpha-oxidation
GO:0006545 glycine biosynthetic process
GO:0006979 response to oxidative stress
GO:0008652 amino acid biosynthetic process
GO:0046296 glycolate catabolic process
Cellular Component
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix
GO:0005829 cytosol
GO:0043231 intracellular membrane-bounded organelle

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2rdw, PDBe:2rdw, PDBj:2rdw
PDBsum2rdw
PubMed18215067
UniProtQ9UJM8|HAOX1_HUMAN 2-Hydroxyacid oxidase 1 (Gene Name=HAO1)

[Back to BioLiP]